Surface structure of the COPII-coated vesicle

被引:93
作者
Matsuoka, K
Schekman, R [1 ]
Orci, L
Heuser, JE
机构
[1] Univ Calif Berkeley, Howard Hughes Med Inst, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[3] Inst Phys & Chem Res, Plant Sci Ctr, Wako, Saitama 3510198, Japan
[4] Univ Geneva, Ctr Med, Dept Morphol, CH-1211 Geneva 4, Switzerland
[5] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63130 USA
关键词
coat proteins; liposome; endoplasmic reticulum membrane; transport vesicle;
D O I
10.1073/pnas.241522198
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The spatial arrangement of COPII coat protein subunits was analyzed by crosslinking to an artificial membrane surface and by electron microscopy of coat proteins and coated vesicle surfaces, The efficiency of COPII subunit crosslinking to phospholipids declined in order of protein recruitment to the coat: Sar1p > Sec23/24p much greater than Sec13/31p. Deep-etch rotary shadowing and electron microscopy were used to explore the COPII subunit structure with isolated proteins and coated vesicles. Sec23/24 resembles a bow tie, and Sec13/31p contains terminal bilobed globular structures bordering a central rod. The surface structure of COPII vesicles revealed a coat built with polygonal units. The length of the side of the hexagonal/pentagonal units is close to the dimension of the central rod-like segment of Sec13/31. Partially uncoated profiles revealed strands of Sec13/31p stripped from the vesicle surface. We conclude that the coat subunits form layers displaced from the membrane surface in reverse order of addition to the coat.
引用
收藏
页码:13705 / 13709
页数:5
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